Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3ZQJ

Mycobacterium tuberculosis UvrA

Replaces: 2YGR

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003677	molecular_function	DNA binding
A	0004518	molecular_function	nuclease activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006281	biological_process	DNA repair
A	0006289	biological_process	nucleotide-excision repair
A	0006974	biological_process	DNA damage response
A	0008270	molecular_function	zinc ion binding
A	0009274	cellular_component	peptidoglycan-based cell wall
A	0009380	cellular_component	excinuclease repair complex
A	0009381	molecular_function	excinuclease ABC activity
A	0009432	biological_process	SOS response
A	0016887	molecular_function	ATP hydrolysis activity
A	0046872	molecular_function	metal ion binding
A	0060543	biological_process	negative regulation of strand invasion
B	0003677	molecular_function	DNA binding
B	0004518	molecular_function	nuclease activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0006281	biological_process	DNA repair
B	0006289	biological_process	nucleotide-excision repair
B	0006974	biological_process	DNA damage response
B	0008270	molecular_function	zinc ion binding
B	0009274	cellular_component	peptidoglycan-based cell wall
B	0009380	cellular_component	excinuclease repair complex
B	0009381	molecular_function	excinuclease ABC activity
B	0009432	biological_process	SOS response
B	0016887	molecular_function	ATP hydrolysis activity
B	0046872	molecular_function	metal ion binding
B	0060543	biological_process	negative regulation of strand invasion
C	0003677	molecular_function	DNA binding
C	0004518	molecular_function	nuclease activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
C	0006281	biological_process	DNA repair
C	0006289	biological_process	nucleotide-excision repair
C	0006974	biological_process	DNA damage response
C	0008270	molecular_function	zinc ion binding
C	0009274	cellular_component	peptidoglycan-based cell wall
C	0009380	cellular_component	excinuclease repair complex
C	0009381	molecular_function	excinuclease ABC activity
C	0009432	biological_process	SOS response
C	0016887	molecular_function	ATP hydrolysis activity
C	0046872	molecular_function	metal ion binding
C	0060543	biological_process	negative regulation of strand invasion
D	0003677	molecular_function	DNA binding
D	0004518	molecular_function	nuclease activity
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0005886	cellular_component	plasma membrane
D	0006281	biological_process	DNA repair
D	0006289	biological_process	nucleotide-excision repair
D	0006974	biological_process	DNA damage response
D	0008270	molecular_function	zinc ion binding
D	0009274	cellular_component	peptidoglycan-based cell wall
D	0009380	cellular_component	excinuclease repair complex
D	0009381	molecular_function	excinuclease ABC activity
D	0009432	biological_process	SOS response
D	0016887	molecular_function	ATP hydrolysis activity
D	0046872	molecular_function	metal ion binding
D	0060543	biological_process	negative regulation of strand invasion
E	0003677	molecular_function	DNA binding
E	0004518	molecular_function	nuclease activity
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0005886	cellular_component	plasma membrane
E	0006281	biological_process	DNA repair
E	0006289	biological_process	nucleotide-excision repair
E	0006974	biological_process	DNA damage response
E	0008270	molecular_function	zinc ion binding
E	0009274	cellular_component	peptidoglycan-based cell wall
E	0009380	cellular_component	excinuclease repair complex
E	0009381	molecular_function	excinuclease ABC activity
E	0009432	biological_process	SOS response
E	0016887	molecular_function	ATP hydrolysis activity
E	0046872	molecular_function	metal ion binding
E	0060543	biological_process	negative regulation of strand invasion
F	0003677	molecular_function	DNA binding
F	0004518	molecular_function	nuclease activity
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0005886	cellular_component	plasma membrane
F	0006281	biological_process	DNA repair
F	0006289	biological_process	nucleotide-excision repair
F	0006974	biological_process	DNA damage response
F	0008270	molecular_function	zinc ion binding
F	0009274	cellular_component	peptidoglycan-based cell wall
F	0009380	cellular_component	excinuclease repair complex
F	0009381	molecular_function	excinuclease ABC activity
F	0009432	biological_process	SOS response
F	0016887	molecular_function	ATP hydrolysis activity
F	0046872	molecular_function	metal ion binding
F	0060543	biological_process	negative regulation of strand invasion

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 1954

Chain	Residue
A	CYS753
A	ALA755
A	CYS756
A	CYS776
A	CYS779

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 1955

Chain	Residue
A	CYS121
A	CYS124
A	CYS257
A	HIS261

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 1956

Chain	Residue
A	CYS282
A	CYS285
A	CYS412
A	CYS415

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 1954

Chain	Residue
B	CYS753
B	CYS756
B	CYS776
B	CYS779

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN B 1955

Chain	Residue
B	CYS121
B	THR123
B	CYS124
B	CYS257
B	HIS261

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 1956

Chain	Residue
B	CYS282
B	CYS285
B	CYS412
B	CYS415

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 1954

Chain	Residue
C	CYS753
C	CYS756
C	CYS776
C	CYS779

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 1955

Chain	Residue
C	CYS282
C	CYS285
C	CYS412
C	CYS415

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 1956

Chain	Residue
C	CYS121
C	CYS124
C	CYS257
C	HIS261

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 1954

Chain	Residue
D	CYS753
D	CYS756
D	CYS776
D	CYS779

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN D 1955

Chain	Residue
D	CYS121
D	THR123
D	CYS124
D	CYS257
D	HIS261

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 1956

Chain	Residue
D	CYS282
D	CYS285
D	CYS412
D	CYS415

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN E 1954

Chain	Residue
E	CYS753
E	CYS756
E	CYS776
E	CYS779

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN E 1955

Chain	Residue
E	CYS282
E	CYS285
E	CYS412
E	VAL414
E	CYS415

Functional Information from PROSITE/UniProt

site_id	PS00211
Number of Residues	15
Details	ABC_TRANSPORTER_1 ABC transporters family signature. LSGGEAQRIRLATQI

Chain	Residue	Details
A	LEU501-ILE515
A	LEU843-LEU857

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	168
Details	ZN_FING: C4-type; atypical => ECO:0000255\|HAMAP-Rule:MF_00205

Chain	Residue	Details
A	CYS257-CYS285
B	CYS257-CYS285
C	CYS257-CYS285
D	CYS257-CYS285
E	CYS257-CYS285
F	CYS257-CYS285

site_id	SWS_FT_FI2
Number of Residues	156
Details	ZN_FING: C4-type => ECO:0000255\|HAMAP-Rule:MF_00205

Chain	Residue	Details
A	CYS753-CYS779
B	CYS753-CYS779
C	CYS753-CYS779
D	CYS753-CYS779
E	CYS753-CYS779
F	CYS753-CYS779

site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00205

Chain	Residue	Details
A	GLY654
D	GLY32
D	GLY654
E	GLY32
E	GLY654
F	GLY32
F	GLY654
A	GLY32
B	GLY32
B	GLY654
C	GLY32
C	GLY654

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)